Research workbench
Crystal structure of degs H198P/D320A mutant modified by dfp in complex with dnrdgnvyyf peptide
Analyse Crystal structure of degs H198P/D320A mutant modified by dfp in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GDS
- Type
- protein
- Length
- 300 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0AEE3
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 296 | — | P0AEE3 |
| B | — | protein | 4 | — | — |
Compared structures
- 3GDS · Crystal structure of DegS H198P/D320A mutant modified by DFP in complex with DNRDGNVYYF… · the same entry in another collection · chain A against A, TM-score 1.00
- P0AEE3 · AlphaFold monomer V2.0 prediction for serine endoprotease degs (P0AEE3) · a predicted model of the same protein · chain A against A, TM-score 0.96
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P0AEE3
- Elsewhere: RCSB PDB 3GDS · PDBe 3GDS · UniProt P0AEE3
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